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J Biol Chem. 2015 May 8;290(19):12147-64. doi: 10.1074/jbc.M115.637694. Epub 2015 Mar 23.

The Plasmodium Class XIV Myosin, MyoB, Has a Distinct Subcellular Location in Invasive and Motile Stages of the Malaria Parasite and an Unusual Light Chain.

Author information

1
From the Divisions of Parasitology.
2
the School of Life Sciences, Queens Medical Centre, University of Nottingham, Nottingham NG2 7UH, United Kingdom.
3
the Institute of Cell Biology, University of Bern, CH-3012 Bern, Switzerland, and.
4
Physical Biochemistry, and.
5
Molecular Structure, MRC National Institute for Medical Research, London NW7 1AA, United Kingdom.
6
the Institute of Chemical Biology, Imperial College London, South Kensington, London SW7 2AZ, United Kingdom.
7
From the Divisions of Parasitology, aholder@nimr.mrc.ac.uk.

Abstract

Myosin B (MyoB) is one of the two short class XIV myosins encoded in the Plasmodium genome. Class XIV myosins are characterized by a catalytic "head," a modified "neck," and the absence of a "tail" region. Myosin A (MyoA), the other class XIV myosin in Plasmodium, has been established as a component of the glideosome complex important in motility and cell invasion, but MyoB is not well characterized. We analyzed the properties of MyoB using three parasite species as follows: Plasmodium falciparum, Plasmodium berghei, and Plasmodium knowlesi. MyoB is expressed in all invasive stages (merozoites, ookinetes, and sporozoites) of the life cycle, and the protein is found in a discrete apical location in these polarized cells. In P. falciparum, MyoB is synthesized very late in schizogony/merogony, and its location in merozoites is distinct from, and anterior to, that of a range of known proteins present in the rhoptries, rhoptry neck or micronemes. Unlike MyoA, MyoB is not associated with glideosome complex proteins, including the MyoA light chain, myosin A tail domain-interacting protein (MTIP). A unique MyoB light chain (MLC-B) was identified that contains a calmodulin-like domain at the C terminus and an extended N-terminal region. MLC-B localizes to the same extreme apical pole in the cell as MyoB, and the two proteins form a complex. We propose that MLC-B is a MyoB-specific light chain, and for the short class XIV myosins that lack a tail region, the atypical myosin light chains may fulfill that role.

KEYWORDS:

Invasion; Malaria; Molecular Motor; Myosin; Myosin Light Chain; Parasite; Peptide Interaction; Plasmodium

PMID:
25802338
PMCID:
PMC4424349
DOI:
10.1074/jbc.M115.637694
[Indexed for MEDLINE]
Free PMC Article

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